Department of Biology, Washington University, Box 1137, 63130, St. Louis, MO, USA.
Plant Cell Rep. 1990 Aug;9(4):211-5. doi: 10.1007/BF00232182.
Two phytases from lily pollen (Lilium longiflorum Thunb.) were partially purified and characterized. The first (pH optimum 5.0) was purified 40-fold from ungerminated pollen. The second (pH optimum 6.5) appeared during germination and was purified 68-fold from pollen germinated 2 h. Molecular weight of the first was 72 kD, and the second was 36 kD as determined by gel filtration. Both were active against phosphate esters other than phytate, although purification of the first reduced its activity against AMP and myo-inositol 2-P to 10% of activity against phytate. Phytase from germinated pollen (but not ungerminated) was inhibited by the sulfhydryl agent parahydroxy mercuribenzoate; P i inhibited phytase from ungerminated but not germinated pollen. Such different catalytic and physical properties may reflect different biochemical functions.
从百合花粉（百合 longiflorum Thunb.）中分离出两种植酸酶，并对其进行了部分纯化和特性分析。第一种（最适 pH 值为 5.0）从未萌发的花粉中纯化了 40 倍。第二种（最适 pH 值为 6.5）在萌发过程中出现，并从萌发 2 小时的花粉中纯化了 68 倍。根据凝胶过滤，第一种的分子量为 72 kD，第二种的分子量为 36 kD。两种酶都能作用于植酸盐以外的磷酸酯，尽管第一种酶的纯化降低了其对 AMP 和肌醇 2-P 的活性，仅为其对植酸盐活性的 10%。发芽花粉中的植酸酶（而非未发芽花粉）被巯基试剂对羟基汞苯甲酸抑制；未发芽花粉中的 P i 抑制植酸酶，但发芽花粉中的 P i 不抑制。这些不同的催化和物理性质可能反映了不同的生化功能。
